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Details on Person Mammalian SWI/SNF complexes are ATP-dependent chromatin remo...

Class:IdSummation:9933243
_displayNameMammalian SWI/SNF complexes are ATP-dependent chromatin remo...
_timestamp2025-02-21 14:54:30
created[InstanceEdit:9933244] Rothfels, Karen, 2024-12-27
modified[InstanceEdit:9933245] Rothfels, Karen, 2024-12-27
[InstanceEdit:9933288] Rothfels, Karen, 2024-12-27
[InstanceEdit:9933410] Rothfels, Karen, 2024-12-30
[InstanceEdit:9933944] Rothfels, Karen, 2025-01-05
[InstanceEdit:9934169] Rothfels, Karen, 2025-01-06
[InstanceEdit:9934292] Rothfels, Karen, 2025-01-07
[InstanceEdit:9938989] Rothfels, Karen, 2025-02-21
textMammalian SWI/SNF complexes are ATP-dependent chromatin remodellers with a central catalytic ATPase consisting of either SMARCA2 (also known as BRM) or SMARCA4 (BRG1), bromodomain-containing proteins that bind acetylated histones (Hassan et al, 2002; Hyun et al, 2024; reviewed in Eustermann et al, 2024). In addition to SMARCA2/4, SWI/SNF complexes also contain varied organizations of 10-14 other proteins, many of which were initially identified as BAFs (BRM/BRG1 associated factors). This module describes the assembly of three well characterized SWI/SNF complexes, the canonical BAF (cBAF), equivalent to the SWI/SNF complex from S. cerevisiae, the polybromo-containing BAF (pBAF) (equivalent to the RSC complex from S. cerevisiae) and the more recently elucidated non-canonical BAF (ncBAF) (He et al, 2020; Mashtalir et al, 2018; Mashtalir et al, 2020; Wang et al, 2022; Yuan et al, 2022; Alpsoy and Dykhuizen, 2018; Michel et al, 2018). All three complexes share catalytic subunits (SMARCA2 or SMARCA4) as well as combinations of 5 other common proteins/protein families (ACTB, ACTL6A/B, BCL7A/B/C, SMARCD1/2/3 and SMARCC1/2) and are additionally distinguished by complex-specific subunits (He et al, 2020; Mashtalir et al, 2018; Wang et al, 2022; Yuan et al, 2022; Alpsoy and Dykhuizen, 2018; Eustermann et al, 2024). In addition to these three complexes, other SWI/SNF complexes have been identified that play tissue-, cell- or developmental-specific roles (see for instance, Lessard et al, 2007; Ho,Ronan et al, 2009; Ho, Jothi et al, 2009; Zhang et al, 2014) but fundamentally all are involved in chromatin assembly or remodelling through alterations of histone-DNA contacts (reviewed in Eustermann et al, 2024; Cenik and Shilatifard, 2021). Mutations in components of SWI/SNF complexes are frequent in cancers and other diseases (Kadoch et al, 2013; reviewed in Mittal and Roberts, 2020; Kadoch and Crabtree, 2015; Cenik and Shilatifard, 2021; Wang and Tang, 2023).
Cryo-EM, cross-linking and gradient sedimentation have revealed the modular organization of mammalian SWI/SNF complexes (He et al, 2020; Mashtalir et al, 2018; Mashtalir et al, 2020). The ATPase module contains most of the catalytic portion of the SMARCA2/4 protein and wraps around the nucleosomal DNA. Closely associated with the catalytic module is a domain consisting of ACTB and ACTL6A/B, as well as SMARCB1 and BCL7 paralogs. A core or base module consisting of the SMARCC dimer and SMARCE1, supplemented by many of the complex-specific subunits, makes contact with the bottom side of the nucleosome (He et al, 2020).
(summation)[Pathway:9932451] SWI/SNF chromatin remodelers [Homo sapiens]
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